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Q8WYB5

- KAT6B_HUMAN

UniProt

Q8WYB5 - KAT6B_HUMAN

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Protein

Histone acetyltransferase KAT6B

Gene

KAT6B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.3 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei891 – 8911Proton donor/acceptorBy similarity
Binding sitei895 – 8951Acetyl-CoABy similarity
Sitei1222 – 12232Breakpoint for translocation to form KAT6B-CREBBP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri213 – 27260PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri269 – 32052PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri749 – 77123C2HC-typeAdd
BLAST

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. DNA binding Source: InterPro
  3. histone acetyltransferase activity Source: UniProtKB
  4. transcription factor binding Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. histone acetylation Source: UniProtKB
  3. histone H3 acetylation Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. nucleosome assembly Source: UniProtKB
  6. positive regulation of transcription, DNA-templated Source: UniProtKB
  7. regulation of transcription, DNA-templated Source: UniProtKB
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.3.1.48. 2681.
ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT6B (EC:2.3.1.481 Publication)
Alternative name(s):
Histone acetyltransferase MOZ2
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4
Short name:
MYST-4
Monocytic leukemia zinc finger protein-related factor
Gene namesi
Name:KAT6B
Synonyms:KIAA0383, MORF, MOZ2, MYST4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:17582. KAT6B.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleosome Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving KAT6B may be a cause acute myeloid leukemias. Translocation t(10;16)(q22;p13) with CREBBP.
Ohdo syndrome, SBBYS variant (SBBYSS) [MIM:603736]: A syndrome characterized by distinctive facial appearance with severe blepharophimosis, an immobile mask-like face, a bulbous nasal tip, and a small mouth with a thin upper lip. The condition presents in infancy with severe hypotonia and feeding problems. Associated skeletal problems include joint laxity, abnormally long thumbs and great toes, and dislocated or hypoplastic patellae. Structural cardiac defects are present in around 50% of cases, and dental anomalies, including small and pointed teeth, are common. Optic atrophy and conductive or sensorineural deafness are repeatedly reported. Many affected individuals have abnormalities of thyroid structure or function. SBBYSS is usually associated with severe mental retardation, delayed motor milestones, and significantly impaired speech.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Genitopatellar syndrome (GTPTS) [MIM:606170]: A rare disorder consisting of microcephaly, severe psychomotor retardation, and characteristic coarse facial features, including broad nose and small or retracted chin, associated with congenital flexion contractures of the lower extremities, abnormal or missing patellae, and urogenital anomalies.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi603736. phenotype.
606170. phenotype.
Orphaneti3047. Blepharophimosis-intellectual disability syndrome, SBBYS type.
85201. Genitopatellar syndrome.
648. Noonan syndrome.
PharmGKBiPA134880712.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20732073Histone acetyltransferase KAT6BPRO_0000051575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei815 – 8151N6-acetyllysine; by autocatalysisBy similarity
Modified residuei1038 – 10381N6-acetyllysine1 Publication
Modified residuei1042 – 10421N6-acetyllysine1 Publication
Modified residuei1044 – 10441N6-acetyllysine1 Publication

Post-translational modificationi

Autoacetylated (PubMed:10497217 and PubMed:11965546). Autoacetylation at Lys-815 is required for proper function.By similarity2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8WYB5.
PaxDbiQ8WYB5.
PRIDEiQ8WYB5.

PTM databases

PhosphoSiteiQ8WYB5.

Expressioni

Tissue specificityi

Ubiquitously expressed, with high levels in heart, pancreas, testis and ovary.1 Publication

Gene expression databases

BgeeiQ8WYB5.
CleanExiHS_MYST4.
ExpressionAtlasiQ8WYB5. baseline and differential.
GenevestigatoriQ8WYB5.

Organism-specific databases

HPAiHPA006104.

Interactioni

Subunit structurei

Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with RUNX1 and RUNX2.3 Publications

Protein-protein interaction databases

BioGridi117069. 10 interactions.
IntActiQ8WYB5. 3 interactions.
MINTiMINT-2871056.
STRINGi9606.ENSP00000287239.

Structurei

3D structure databases

ProteinModelPortaliQ8WYB5.
SMRiQ8WYB5. Positions 211-320, 718-990.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 17674H15PROSITE-ProRule annotationAdd
BLAST
Domaini715 – 989275MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni361 – 717357Negatively regulates HAT activityAdd
BLAST
Regioni718 – 1008291CatalyticAdd
BLAST
Regioni752 – 1008257Interaction with BRPF1Add
BLAST
Regioni856 – 8605Acetyl-CoA bindingBy similarity
Regioni865 – 8717Acetyl-CoA bindingBy similarity
Regioni1560 – 2073514Interaction with RUNX1 and RUNX2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi492 – 53342Ser-richAdd
BLAST
Compositional biasi521 – 5244Poly-Ser
Compositional biasi599 – 6057Poly-Ser
Compositional biasi1070 – 110435Poly-GluAdd
BLAST
Compositional biasi1204 – 12074Poly-Glu
Compositional biasi1351 – 137323Poly-GluAdd
BLAST
Compositional biasi1409 – 14179Poly-Glu
Compositional biasi1594 – 1763170Ser-richAdd
BLAST
Compositional biasi1961 – 2061101Met-richAdd
BLAST

Domaini

The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression.1 Publication

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC-type zinc finger.Curated
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri213 – 27260PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri269 – 32052PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri749 – 77123C2HC-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00550000074503.
HOVERGENiHBG052563.
InParanoidiQ8WYB5.
KOiK11306.
OMAiLRWTPIL.
OrthoDBiEOG7WHH8N.
PhylomeDBiQ8WYB5.
TreeFamiTF106483.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.40.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011991. WHTH_DNA-bd_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8WYB5-1) [UniParc]FASTAAdd to Basket

Also known as: Beta

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ
60 70 80 90 100
LELSVQDGSV LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK SAKGSRGSCN
110 120 130 140 150
DLRNVDWNKL LRRAIEGLEE PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ
160 170 180 190 200
RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD GKGAPQYPSA FPSSLPPVSL
210 220 230 240 250
LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC GSSGHPSCLK
260 270 280 290 300
FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC
310 320 330 340 350
DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK
360 370 380 390 400
QRLLSVTSDE GSMNAFTGRG SPGRGQKTKV CTTPSSGHAA SGKDSSSRLA
410 420 430 440 450
VTDPTRPGAT TKITTTSTYI SASTLKVNKK TKGLIDGLTK FFTPSPDGRR
460 470 480 490 500
SRGEIIDFSK HYRPRKKVSQ KQSCTSHVLA TGTTQKLKPP PSSLPPPTPI
510 520 530 540 550
SGQSPSSQKS STATSSPSPQ SSSSQCSVPS LSSLTTNSQL KALFDGLSHI
560 570 580 590 600
YTTQGQSRKK GHPSYAPPKR MRRKTELSST AKSKAHFFGK RDIRSRFISH
610 620 630 640 650
SSSSSWGMAR GSIFKAIAHF KRTTFLKKHR MLGRLKYKVT PQMGTPSPGK
660 670 680 690 700
GSLTDGRIKP DQDDDTEIKI NIKQESADVN VIGNKDVVTE EDLDVFKQAQ
710 720 730 740 750
ELSWEKIECE SGVEDCGRYP SVIEFGKYEI QTWYSSPYPQ EYARLPKLYL
760 770 780 790 800
CEFCLKYMKS KNILLRHSKK CGWFHPPANE IYRRKDLSVF EVDGNMSKIY
810 820 830 840 850
CQNLCLLAKL FLDHKTLYYD VEPFLFYVLT KNDEKGCHLV GYFSKEKLCQ
860 870 880 890 900
QKYNVSCIMI MPQHQRQGFG RFLIDFSYLL SRREGQAGSP EKPLSDLGRL
910 920 930 940 950
SYLAYWKSVI LEYLYHHHER HISIKAISRA TGMCPHDIAT TLQHLHMIDK
960 970 980 990 1000
RDGRFVIIRR EKLILSHMEK LKTCSRANEL DPDSLRWTPI LISNAAVSEE
1010 1020 1030 1040 1050
EREAEKEAER LMEQASCWEK EEQEILSTRA NSRQSPAKVQ SKNKYLHSPE
1060 1070 1080 1090 1100
SRPVTGERGQ LLELSKESSE EEEEEEDEEE EEEEEEEEED EEEEEEEEEE
1110 1120 1130 1140 1150
EEEENIQSSP PRLTKPQSVA IKRKRPFVLK KKRGRKRRRI NSSVTTETIS
1160 1170 1180 1190 1200
ETTEVLNEPF DNSDEERPMP QLEPTCEIEV EEDGRKPVLR KAFQHQPGKK
1210 1220 1230 1240 1250
RQTEEEEGKD NHCFKNADPC RNNMNDDSSN LKEGSKDNPE PLKCKQVWPK
1260 1270 1280 1290 1300
GTKRGLSKWR QNKERKTGFK LNLYTPPETP MEPDEQVTVE EQKETSEGKT
1310 1320 1330 1340 1350
SPSPIRIEEE VKETGEALLP QEENRREETC APVSPNTSPG EKPEDDLIKP
1360 1370 1380 1390 1400
EEEEEEEEEE EEEEEEEEGE EEEGGGNVEK DPDGAKSQEK EEPEISTEKE
1410 1420 1430 1440 1450
DSARLDDHEE EEEEDEEPSH NEDHDADDED DSHMESAEVE KEELPRESFK
1460 1470 1480 1490 1500
EVLENQETFL DLNVQPGHSN PEVLMDCGVD LTASCNSEPK ELAGDPEAVP
1510 1520 1530 1540 1550
ESDEEPPPGE QAQKQDQKNS KEVDTEFKEG NPATMEIDSE TVQAVQSLTQ
1560 1570 1580 1590 1600
ESSEQDDTFQ DCAETQEACR SLQNYTRADQ SPQIATTLDD CQQSDHSSPV
1610 1620 1630 1640 1650
SSVHSHPGQS VRSVNSPSVP ALENSYAQIS PDQSAISVPS LQNMETSPMM
1660 1670 1680 1690 1700
DVPSVSDHSQ QVVDSGFSDL GSIESTTENY ENPSSYDSTM GGSICGNGSS
1710 1720 1730 1740 1750
QNSCSYSNLT SSSLTQSSCA VTQQMSNISG SCSMLQQTSI SSPPTCSVKS
1760 1770 1780 1790 1800
PQGCVVERPP SSSQQLAQCS MAANFTPPMQ LAEIPETSNA NIGLYERMGQ
1810 1820 1830 1840 1850
SDFGAGHYPQ PSATFSLAKL QQLTNTLIDH SLPYSHSAAV TSYANSASLS
1860 1870 1880 1890 1900
TPLSNTGLVQ LSQSPHSVPG GPQAQATMTP PPNLTPPPMN LPPPLLQRNM
1910 1920 1930 1940 1950
AASNIGISHS QRLQTQIASK GHISMRTKSA SLSPAAATHQ SQIYGRSQTV
1960 1970 1980 1990 2000
AMQGPARTLT MQRGMNMSVN LMPAPAYNVN SVNMNMNTLN AMNGYSMSQP
2010 2020 2030 2040 2050
MMNSGYHSNH GYMNQTPQYP MQMQMGMMGT QPYAQQPMQT PPHGNMMYTA
2060 2070
PGHHGYMNTG MSKQSLNGSY MRR
Length:2,073
Mass (Da):231,378
Last modified:April 3, 2007 - v3
Checksum:iAEE267B9DA444B08
GO
Isoform 2 (identifier: Q8WYB5-2) [UniParc]FASTAAdd to Basket

Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     482-664: Missing.

Show »
Length:1,890
Mass (Da):211,537
Checksum:i9AD95D653693CFBA
GO
Isoform 3 (identifier: Q8WYB5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     373-664: Missing.

Show »
Length:1,781
Mass (Da):199,858
Checksum:i895F7DE8B12455E8
GO

Sequence cautioni

The sequence AAH14143.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH48199.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAF00100.1 differs from that shown. Reason: Frameshift at positions 550 and 562.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1231G → R in AAL56647. 1 PublicationCurated
Sequence conflicti231 – 2311P → A in AAL56647. 1 PublicationCurated
Sequence conflicti843 – 8431F → L in AAF00095. (PubMed:10497217)Curated
Sequence conflicti843 – 8431F → L in AAF00099. (PubMed:10497217)Curated
Sequence conflicti843 – 8431F → L in AAF00100. (PubMed:10497217)Curated
Sequence conflicti843 – 8431F → L in BAA20837. (PubMed:9205841)Curated
Sequence conflicti931 – 9333TGM → RHV in AAL56647. 1 PublicationCurated
Sequence conflicti934 – 9341Missing in AAL56647. 1 PublicationCurated
Sequence conflicti1152 – 11521T → S in AAL56647. 1 PublicationCurated
Sequence conflicti1625 – 16251S → T in AAL56647. 1 PublicationCurated
Sequence conflicti1731 – 17311S → T in AAL56647. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti360 – 3601E → K.1 Publication
VAR_067315
Natural varianti483 – 4831T → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_036361
Natural varianti1217 – 12171A → S.
Corresponds to variant rs57372986 [ dbSNP | Ensembl ].
VAR_061367
Natural varianti1499 – 14991V → I.
Corresponds to variant rs3740321 [ dbSNP | Ensembl ].
VAR_050217

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei373 – 664292Missing in isoform 3. 2 PublicationsVSP_014586Add
BLAST
Alternative sequencei482 – 664183Missing in isoform 2. 1 PublicationVSP_014587Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF113514 mRNA. Translation: AAF00095.1.
AF119230 mRNA. Translation: AAF00099.1.
AF119231 mRNA. Translation: AAF00100.1. Frameshift.
AF217500 mRNA. Translation: AAL56647.1.
AB002381 mRNA. Translation: BAA20837.2.
BC014143 mRNA. Translation: AAH14143.1. Sequence problems.
BC021128 mRNA. Translation: AAH21128.1.
BC048199 mRNA. Translation: AAH48199.1. Sequence problems.
CCDSiCCDS58084.1. [Q8WYB5-3]
CCDS58085.1. [Q8WYB5-2]
CCDS7345.1. [Q8WYB5-1]
RefSeqiNP_001243397.1. NM_001256468.1. [Q8WYB5-2]
NP_001243398.1. NM_001256469.1. [Q8WYB5-3]
NP_036462.2. NM_012330.3. [Q8WYB5-1]
XP_005269721.1. XM_005269664.1. [Q8WYB5-1]
UniGeneiHs.35758.
Hs.599543.
Hs.740873.

Genome annotation databases

EnsembliENST00000287239; ENSP00000287239; ENSG00000156650. [Q8WYB5-1]
ENST00000372711; ENSP00000361796; ENSG00000156650. [Q8WYB5-2]
ENST00000372714; ENSP00000361799; ENSG00000156650. [Q8WYB5-3]
ENST00000372724; ENSP00000361809; ENSG00000156650. [Q8WYB5-3]
ENST00000372725; ENSP00000361810; ENSG00000156650. [Q8WYB5-3]
GeneIDi23522.
KEGGihsa:23522.
UCSCiuc001jwm.2. human. [Q8WYB5-3]
uc001jwn.2. human. [Q8WYB5-1]
uc031pvy.1. human. [Q8WYB5-2]

Polymorphism databases

DMDMi143811424.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF113514 mRNA. Translation: AAF00095.1 .
AF119230 mRNA. Translation: AAF00099.1 .
AF119231 mRNA. Translation: AAF00100.1 . Frameshift.
AF217500 mRNA. Translation: AAL56647.1 .
AB002381 mRNA. Translation: BAA20837.2 .
BC014143 mRNA. Translation: AAH14143.1 . Sequence problems.
BC021128 mRNA. Translation: AAH21128.1 .
BC048199 mRNA. Translation: AAH48199.1 . Sequence problems.
CCDSi CCDS58084.1. [Q8WYB5-3 ]
CCDS58085.1. [Q8WYB5-2 ]
CCDS7345.1. [Q8WYB5-1 ]
RefSeqi NP_001243397.1. NM_001256468.1. [Q8WYB5-2 ]
NP_001243398.1. NM_001256469.1. [Q8WYB5-3 ]
NP_036462.2. NM_012330.3. [Q8WYB5-1 ]
XP_005269721.1. XM_005269664.1. [Q8WYB5-1 ]
UniGenei Hs.35758.
Hs.599543.
Hs.740873.

3D structure databases

ProteinModelPortali Q8WYB5.
SMRi Q8WYB5. Positions 211-320, 718-990.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117069. 10 interactions.
IntActi Q8WYB5. 3 interactions.
MINTi MINT-2871056.
STRINGi 9606.ENSP00000287239.

PTM databases

PhosphoSitei Q8WYB5.

Polymorphism databases

DMDMi 143811424.

Proteomic databases

MaxQBi Q8WYB5.
PaxDbi Q8WYB5.
PRIDEi Q8WYB5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000287239 ; ENSP00000287239 ; ENSG00000156650 . [Q8WYB5-1 ]
ENST00000372711 ; ENSP00000361796 ; ENSG00000156650 . [Q8WYB5-2 ]
ENST00000372714 ; ENSP00000361799 ; ENSG00000156650 . [Q8WYB5-3 ]
ENST00000372724 ; ENSP00000361809 ; ENSG00000156650 . [Q8WYB5-3 ]
ENST00000372725 ; ENSP00000361810 ; ENSG00000156650 . [Q8WYB5-3 ]
GeneIDi 23522.
KEGGi hsa:23522.
UCSCi uc001jwm.2. human. [Q8WYB5-3 ]
uc001jwn.2. human. [Q8WYB5-1 ]
uc031pvy.1. human. [Q8WYB5-2 ]

Organism-specific databases

CTDi 23522.
GeneCardsi GC10P076586.
GeneReviewsi KAT6B.
HGNCi HGNC:17582. KAT6B.
HPAi HPA006104.
MIMi 603736. phenotype.
605880. gene.
606170. phenotype.
neXtProti NX_Q8WYB5.
Orphaneti 3047. Blepharophimosis-intellectual disability syndrome, SBBYS type.
85201. Genitopatellar syndrome.
648. Noonan syndrome.
PharmGKBi PA134880712.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5027.
GeneTreei ENSGT00550000074503.
HOVERGENi HBG052563.
InParanoidi Q8WYB5.
KOi K11306.
OMAi LRWTPIL.
OrthoDBi EOG7WHH8N.
PhylomeDBi Q8WYB5.
TreeFami TF106483.

Enzyme and pathway databases

BRENDAi 2.3.1.48. 2681.
Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi KAT6B. human.
GeneWikii MYST4.
GenomeRNAii 23522.
NextBioi 45977.
PROi Q8WYB5.
SOURCEi Search...

Gene expression databases

Bgeei Q8WYB5.
CleanExi HS_MYST4.
ExpressionAtlasi Q8WYB5. baseline and differential.
Genevestigatori Q8WYB5.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.30.40.10. 1 hit.
3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011991. WHTH_DNA-bd_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF00538. Linker_histone. 1 hit.
PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEi PS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein."
    Champagne N., Bertos N.R., Pelletier N., Wang A.H., Vezmar M., Yang Y., Heng H.H., Yang X.-J.
    J. Biol. Chem. 274:28528-28536(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AUTOACETYLATION, CATALYTIC ACTIVITY, DOMAIN, FUNCTION.
    Tissue: Bone marrow.
  2. "Structure and function of the human MYST family: MOZ2, MYST1 and MYST2."
    Borrow J., Housman D.E.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-322 AND 1187-2073.
    Tissue: Brain and Lung.
  6. "Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13)."
    Panagopoulos I., Fioretos T., Isaksson M., Samuelsson U., Billstroem R., Stroembeck B., Mitelman F., Johansson B.
    Hum. Mol. Genet. 10:395-404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1136-1287, CHROMOSOMAL TRANSLOCATION WITH CREBBP.
  7. "MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2."
    Pelletier N., Champagne N., Stifani S., Yang X.-J.
    Oncogene 21:2729-2740(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RUNX1 AND RUNX2, AUTOACETYLATION, FUNCTION.
  8. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
    Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
    Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
  9. Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1038; LYS-1042 AND LYS-1044, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Whole-exome-sequencing identifies mutations in histone acetyltransferase gene KAT6B in individuals with the Say-Barber-Biesecker variant of Ohdo syndrome."
    Clayton-Smith J., O'Sullivan J., Daly S., Bhaskar S., Day R., Anderson B., Voss A.K., Thomas T., Biesecker L.G., Smith P., Fryer A., Chandler K.E., Kerr B., Tassabehji M., Lynch S.A., Krajewska-Walasek M., McKee S., Smith J.
    , Sweeney E., Mansour S., Mohammed S., Donnai D., Black G.
    Am. J. Hum. Genet. 89:675-681(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SBBYSS, VARIANT LYS-360.
  12. Cited for: INVOLVEMENT IN GTPTS.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-483.

Entry informationi

Entry nameiKAT6B_HUMAN
AccessioniPrimary (citable) accession number: Q8WYB5
Secondary accession number(s): O15087
, Q86Y05, Q8WU81, Q9UKW2, Q9UKW3, Q9UKX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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